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R H Burris

Publications and source records attributed to R H Burris.

At least 109 records · Page 6Linked to original sources
PubMed1973

A comparison of the physical and chemical properties of four cytochromes c from Azotobacter vinelandii.

1. A modified method for the separation and purification of four cytochromes c from Azotobacter vinelandii is described. Two new cytochromes c have been purified and are designated cytochromes c(551) and c(555). 2. Additional evidence is presented to establish the dihaem nature of cytochrome c(4). Ultracentrifugation data indicated similar molecular weights for the native and the denatured protein. Cleavage with CNBr yielded seven peptides; the amino acid compositions of the purified peptides were determined. Only one haem peptide was recovered. 3. Cytochromes c(551) and c(555) were characterized as acidic proteins of molecular weights about 12000. The spectral properties, isoelectric points, ;maps' of peptides from CNBr cleavage and amino acid compositions were determined for these two proteins. 4. The spectral properties, isoelectric points, molecular weights, CNBr peptide ;maps', amino acid compositions, relative oxidation-reduction potentials and e.p.r. (electron-paramagnetic-resonance) spectra of the four cytochromes c were compared. Cytochrome c(4) and cytochrome c(551) appear to be distinct proteins. The distinction between cytochromes c(5) and c(555) was not as clear, and our data are inadequate to establish firmly that they are distinct proteins. 5. The dihaem nature of cytochrome c(4) is evident in its e.p.r. spectrum. The e.p.r. spectra are similar to the spectra of mammalian cytochromes c.

Amino Acid Sequence↗
PubMed1972

Electron paramagnetic resonance of nitrogenase and nitrogenase components from Clostridium pasteurianum W5 and Azotobacter vinelandii OP.

The electron paramagnetic resonance of nitrogenase components, separately and together with the other reactants in the nitrogenase system (namely, reductant and Mg.ATP), have been examined at low temperatures (<20 degrees K). The MoFe protein, component I or molybdoferredoxin, in the oxidized (but not oxygen-inactivated) state yields signals with g-values of 4.3, 3.7, and 2.01, and when reduced has no observable electron paramagnetic resonance. The Fe protein, component II, or azoferredoxin, yields a signal with g-values of 2.05, 1.94, and 1.89 in the reduced state that is converted by Mg.ATP into an axial signal with g-values near 2.05 and 1.94, and a second split signal near g = 4.3. The Fe protein has no definite electron paramagnetic resonance in the oxidized (not oxygen-denatured) state under these conditions. The Mg.ATP complex of reduced Fe protein reduces the MoFe protein, whereas dithionite alone does not reduce the MoFe protein. Reoxidation of the system by substrate leads to disappearance of the Fe protein signal and the reappearance of the MoFe protein signal. Thus Mg.ATP, which is hydrolyzed during substrate reduction, converts the Fe protein to a reductant capable of transferring electrons to MoFe protein, after which substrate reduction occurs.

Adenosine Triphosphate↗
PubMed1972

Nature of oxygen inhibition of nitrogenase from Azotobacter vinelandii.

The reduction of nitrogen, acetylene, azide, and cyanide at various oxygen concentrations by nitrogenase from Azotobacter vinelandii was measured with a well-defined system. Oxygen inhibited the reduction of each substrate uncompetitively. The inhibition constants (K(i)) were 0.014, 0.023, 0.008, and 0.003 atm of oxygen for reduction of nitrogen, acetylene, azide, and cyanide, respectively. The system used included ATP-generating components, subcellular particles from A. vinelandii with high nitrogenase specific activity, and illuminated spinach chloroplasts plus carriers to supply electrons. Oxygen did not affect the photochemical electron donating system, but it did inhibit nitrogenase-dependent ATP hydrolysis.

Acetylene↗
PubMed1970

Acetylene reduction assay for determination of phosphorus availability in wisconsin lakes.

Phosphorus-starved cells of Anabaena flos-aquae rapidly increase their capacity to reduce acetylene to ethylene when they receive phosphorus. This response may be used as a bioassay for detecting available phosphorus in aquatic ecosystems. The sensitivity of the method compares favorably with conventional methods for measuring dissolved orthophosphate, and has the additional advantage that it measures available phosphorus. Studies on Wisconsin lakes show that available phosphorus generally is present, that the concentrations are higher at the lower depths than at the surface, and that there may be diurnal variations in the available phosphorus content of surface waters. Important sources of available phosphorus in Lake Mendota are the waters below the thermocline and the input from storm sewers.

Journal Article↗
PubMed1970

Purification and properties of the constituents of the nitrogenase complex from Clostridium pasteurianum.

A new procedure for a rapid and extensive purification of the FeMo protein and the Fe protein of the nitrogenase complex from Clostridium pasteurianum is described. Specific activities of 345 and 460 nmoles of N(2) reduced per mg of protein per min for the FeMo protein and for the Fe protein, respectively, have been obtained. Preparations of the FeMo protein contained 0.96 atom of molybdenum and 15 atoms of iron per molecule, whereas those of the Fe protein contained 2.86 atoms of iron per molecule. Experiments suggest that a definite association of two Fe proteins and one FeMo protein is functional in the active enzyme complex. No individual role could be ascribed to either of the two proteins, but the fact that hydrogenase inhibits N(2) fixation but not the reductant-dependent adenosine triphosphate hydrolysis supports the idea that there are two distinct sites on nitrogenase, one concerned with N(2) activation and the other with activated electron transport.

Bacterial Proteins↗
PubMed1969

Cytokinin activation of de novo thiamine biosynthesis in tobacco callus cultures.

The effect of kinetin on the de novo formation of thiamine in tobacco callus cultures was measured by following the isotope dilution of previously introduced (14)C-thiamine. Thiamine was determined by the thiochrome fluorescence assay after chromatographic purification. Morphological effects induced by high kinetin concentrations were visible within a week after tissue transfer, but thiamine synthesis was insignificant for 2 weeks both in cultures with high (1000 mug/l) and low (30 mug/l) kinetin treatments. Thiamine synthesis during the third week was observed at both kinetin levels, the high kinetin treatment supporting 2.5 times the thiamine synthesis of the low kinetin treatment. The kinetin induced increases in thiamine observed earlier by Digby and Skoog apparently resulted from stimulation of thiamine synthesis rather than from sparing its destruction. Thiamine synthesis is initiated when thiamine concentration reaches a minimum in the callus tissue. This suggests that kinetin is required for the synthesis, but that the activation of synthesis is under feedback control sensitive to the level of thiamine in the tissue.

Culture Techniques↗